3RRW
Crystal structure of the TL29 protein from Arabidopsis thaliana
3RRW の概要
| エントリーDOI | 10.2210/pdb3rrw/pdb |
| 分子名称 | Thylakoid lumenal 29 kDa protein, chloroplastic, PHOSPHATE ION, CALCIUM ION, ... (5 entities in total) |
| 機能のキーワード | chloroplast thylakoid lumen, plant protein |
| 由来する生物種 | Arabidopsis thaliana (mouse-ear cress, thale-cress) |
| 細胞内の位置 | Plastid, chloroplast thylakoid lumen : P82281 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 60026.42 |
| 構造登録者 | Lundberg, E.,Storm, P.,Schroder, W.P.,Funk, C. (登録日: 2011-05-01, 公開日: 2011-08-03, 最終更新日: 2024-10-16) |
| 主引用文献 | Lundberg, E.,Storm, P.,Schroder, W.P.,Funk, C. Crystal structure of the TL29 protein from Arabidopsis thaliana: An APX homolog without peroxidase activity. J.Struct.Biol., 176:24-31, 2011 Cited by PubMed Abstract: TL29 is a plant-specific protein found in the thylakoid lumen of chloroplasts. Despite the putative requirement in plants for a peroxidase close to the site of photosynthetic oxygen production, and the sequence homology of TL29 to ascorbate peroxidases, so far biochemical methods have not shown this enzyme to possess peroxidase activity. Here we report the three-dimensional X-ray crystal structure of recombinant TL29 from Arabidopsis thaliana at a resolution of 2.5Å. The overall structure of TL29 is mainly alpha helical with six longer and six shorter helical segments. The TL29 structure resembles that of typical ascorbate peroxidases, however, crucial differences were found in regions that would be important for heme and ascorbate binding. Such differences suggest it to be highly unlikely that TL29 functions as a peroxidase. PubMed: 21798352DOI: 10.1016/j.jsb.2011.07.004 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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